Dynamic Forcing, a Method for Evaluating Activity and Selectivity Profiles of RGD (Arg‐Gly‐Asp) Peptides | Zendy

Müller Gerhard | Zendy; Gurrath Marion | Zendy; Kessler Horst | Zendy; Timpl Rupert | Zendy

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Dynamic Forcing, a Method for Evaluating Activity and Selectivity Profiles of RGD (Arg‐Gly‐Asp) Peptides

Author(s) -

Müller Gerhard,

Gurrath Marion,

Kessler Horst,

Timpl Rupert

Publication year - 1992

Publication title -

angewandte chemie international edition in english

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 0570-0833

DOI - 10.1002/anie.199203261

Subject(s) - selectivity , forcing (mathematics) , receptor , chemistry , molecular dynamics , stereochemistry , peptide , biophysics , computational chemistry , biochemistry , physics , biology , atmospheric sciences , catalysis

The easy interconversion between two conformations , which is deduced from molecular dynamics simulations, explains why the cyclopeptide 1 is equally well bound to two receptors whereas the very similar cyclopeptide 2 shows a selectivity towards these receptors of ca. 30:1. The method of “dynamic forcing” showed that 1 can very easily be transformed from its most stable conformation into a conformation which corresponds to that of 2 . Thus, for the first time a connection between the biological activity of a compound and its conformational freedom has been established.

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